[{"year":"2018","intvolume":"        19","date_updated":"2023-02-23T13:28:52Z","date_published":"2018-12-27T00:00:00Z","doi":"10.1186/s12864-018-5245-1","article_number":"965","publication":"BMC Genomics","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"full_name":"Bochkareva, Olga","orcid":"0000-0003-1006-6639","last_name":"Bochkareva","first_name":"Olga","id":"C4558D3C-6102-11E9-A62E-F418E6697425"},{"first_name":"Elena V.","last_name":"Moroz","full_name":"Moroz, Elena V."},{"first_name":"Iakov I.","full_name":"Davydov, Iakov I.","last_name":"Davydov"},{"first_name":"Mikhail S.","last_name":"Gelfand","full_name":"Gelfand, Mikhail S."}],"publication_identifier":{"issn":["1471-2164"]},"month":"12","language":[{"iso":"eng"}],"day":"27","type":"journal_article","oa_version":"Published Version","status":"public","publication_status":"published","article_processing_charge":"No","title":"Genome rearrangements and selection in multi-chromosome bacteria Burkholderia spp.","article_type":"original","extern":"1","oa":1,"_id":"8262","citation":{"ista":"Bochkareva O, Moroz EV, Davydov II, Gelfand MS. 2018. Genome rearrangements and selection in multi-chromosome bacteria Burkholderia spp. BMC Genomics. 19, 965.","ieee":"O. Bochkareva, E. V. Moroz, I. I. Davydov, and M. S. Gelfand, “Genome rearrangements and selection in multi-chromosome bacteria Burkholderia spp.,” <i>BMC Genomics</i>, vol. 19. Springer Nature, 2018.","apa":"Bochkareva, O., Moroz, E. V., Davydov, I. I., &#38; Gelfand, M. S. (2018). Genome rearrangements and selection in multi-chromosome bacteria Burkholderia spp. <i>BMC Genomics</i>. Springer Nature. <a href=\"https://doi.org/10.1186/s12864-018-5245-1\">https://doi.org/10.1186/s12864-018-5245-1</a>","ama":"Bochkareva O, Moroz EV, Davydov II, Gelfand MS. Genome rearrangements and selection in multi-chromosome bacteria Burkholderia spp. <i>BMC Genomics</i>. 2018;19. doi:<a href=\"https://doi.org/10.1186/s12864-018-5245-1\">10.1186/s12864-018-5245-1</a>","short":"O. Bochkareva, E.V. Moroz, I.I. Davydov, M.S. Gelfand, BMC Genomics 19 (2018).","mla":"Bochkareva, Olga, et al. “Genome Rearrangements and Selection in Multi-Chromosome Bacteria Burkholderia Spp.” <i>BMC Genomics</i>, vol. 19, 965, Springer Nature, 2018, doi:<a href=\"https://doi.org/10.1186/s12864-018-5245-1\">10.1186/s12864-018-5245-1</a>.","chicago":"Bochkareva, Olga, Elena V. Moroz, Iakov I. Davydov, and Mikhail S. Gelfand. “Genome Rearrangements and Selection in Multi-Chromosome Bacteria Burkholderia Spp.” <i>BMC Genomics</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1186/s12864-018-5245-1\">https://doi.org/10.1186/s12864-018-5245-1</a>."},"publisher":"Springer Nature","date_created":"2020-08-15T11:02:08Z","quality_controlled":"1","main_file_link":[{"open_access":"1","url":"https://doi.org/10.1186/s12864-018-5245-1"}],"volume":19,"abstract":[{"lang":"eng","text":"Background: The genus Burkholderia consists of species that occupy remarkably diverse ecological niches. Its best known members are important pathogens, B. mallei and B. pseudomallei, which cause glanders and melioidosis, respectively. Burkholderia genomes are unusual due to their multichromosomal organization, generally comprised of 2-3 chromosomes.\r\n\r\nResults: We performed integrated genomic analysis of 127 Burkholderia strains. The pan-genome is open with the saturation to be reached between 86,000 and 88,000 genes. The reconstructed rearrangements indicate a strong avoidance of intra-replichore inversions that is likely caused by selection against the transfer of large groups of genes between the leading and the lagging strands. Translocated genes also tend to retain their position in the leading or the lagging strand, and this selection is stronger for large syntenies. Integrated reconstruction of chromosome rearrangements in the context of strains phylogeny reveals parallel rearrangements that may indicate inversion-based phase variation and integration of new genomic islands. In particular, we detected parallel inversions in the second chromosomes of B. pseudomallei with breakpoints formed by genes encoding membrane components of multidrug resistance complex, that may be linked to a phase variation mechanism. Two genomic islands, spreading horizontally between chromosomes, were detected in the B. cepacia group.\r\n\r\nConclusions: This study demonstrates the power of integrated analysis of pan-genomes, chromosome rearrangements, and selection regimes. Non-random inversion patterns indicate selective pressure, inversions are particularly frequent in a recent pathogen B. mallei, and, together with periods of positive selection at other branches, may indicate adaptation to new niches. One such adaptation could be a possible phase variation mechanism in B. pseudomallei."}]},{"oa_version":"Published Version","type":"journal_article","volume":6,"abstract":[{"lang":"eng","text":"Genome rearrangements have played an important role in the evolution of Yersinia pestis from its progenitor Yersinia pseudotuberculosis. Traditional phylogenetic trees for Y. pestis based on sequence comparison have short internal branches and low bootstrap supports as only a small number of nucleotide substitutions have occurred. On the other hand, even a small number of genome rearrangements may resolve topological ambiguities in a phylogenetic tree. We reconstructed phylogenetic trees based on genome rearrangements using several popular approaches such as Maximum likelihood for Gene Order and the Bayesian model of genome rearrangements by inversions. We also reconciled phylogenetic trees for each of the three CRISPR loci to obtain an integrated scenario of the CRISPR cassette evolution. Analysis of contradictions between the obtained evolutionary trees yielded numerous parallel inversions and gain/loss events. Our data indicate that an integrated analysis of sequence-based and inversion-based trees enhances the resolution of phylogenetic reconstruction. In contrast, reconstructions of strain relationships based on solely CRISPR loci may not be reliable, as the history is obscured by large deletions, obliterating the order of spacer gains. Similarly, numerous parallel gene losses preclude reconstruction of phylogeny based on gene content."}],"_id":"8265","intvolume":"         6","date_published":"2018-03-27T00:00:00Z","day":"27","language":[{"iso":"eng"}],"publication":"PeerJ","publication_identifier":{"issn":["2167-8359"]},"title":"Genome rearrangements and phylogeny reconstruction in Yersinia pestis","article_processing_charge":"No","extern":"1","article_type":"original","status":"public","publication_status":"published","quality_controlled":"1","main_file_link":[{"url":"https://doi.org/10.7717/peerj.4545","open_access":"1"}],"date_created":"2020-08-15T11:08:23Z","publisher":"PeerJ","citation":{"chicago":"Bochkareva, Olga, Natalia O. Dranenko, Elena S. Ocheredko, German M. Kanevsky, Yaroslav N. Lozinsky, Vera A. Khalaycheva, Irena I. Artamonova, and Mikhail S. Gelfand. “Genome Rearrangements and Phylogeny Reconstruction in Yersinia Pestis.” <i>PeerJ</i>. PeerJ, 2018. <a href=\"https://doi.org/10.7717/peerj.4545\">https://doi.org/10.7717/peerj.4545</a>.","mla":"Bochkareva, Olga, et al. “Genome Rearrangements and Phylogeny Reconstruction in Yersinia Pestis.” <i>PeerJ</i>, vol. 6, e4545, PeerJ, 2018, doi:<a href=\"https://doi.org/10.7717/peerj.4545\">10.7717/peerj.4545</a>.","short":"O. Bochkareva, N.O. Dranenko, E.S. Ocheredko, G.M. Kanevsky, Y.N. Lozinsky, V.A. Khalaycheva, I.I. Artamonova, M.S. Gelfand, PeerJ 6 (2018).","ama":"Bochkareva O, Dranenko NO, Ocheredko ES, et al. Genome rearrangements and phylogeny reconstruction in Yersinia pestis. <i>PeerJ</i>. 2018;6. doi:<a href=\"https://doi.org/10.7717/peerj.4545\">10.7717/peerj.4545</a>","apa":"Bochkareva, O., Dranenko, N. O., Ocheredko, E. S., Kanevsky, G. M., Lozinsky, Y. N., Khalaycheva, V. A., … Gelfand, M. S. (2018). Genome rearrangements and phylogeny reconstruction in Yersinia pestis. <i>PeerJ</i>. PeerJ. <a href=\"https://doi.org/10.7717/peerj.4545\">https://doi.org/10.7717/peerj.4545</a>","ieee":"O. Bochkareva <i>et al.</i>, “Genome rearrangements and phylogeny reconstruction in Yersinia pestis,” <i>PeerJ</i>, vol. 6. PeerJ, 2018.","ista":"Bochkareva O, Dranenko NO, Ocheredko ES, Kanevsky GM, Lozinsky YN, Khalaycheva VA, Artamonova II, Gelfand MS. 2018. Genome rearrangements and phylogeny reconstruction in Yersinia pestis. PeerJ. 6, e4545."},"oa":1,"date_updated":"2023-02-23T13:28:57Z","doi":"10.7717/peerj.4545","year":"2018","month":"03","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_number":"e4545","external_id":{"pmid":["29607260"]},"pmid":1,"author":[{"first_name":"Olga","id":"C4558D3C-6102-11E9-A62E-F418E6697425","orcid":"0000-0003-1006-6639","full_name":"Bochkareva, Olga","last_name":"Bochkareva"},{"first_name":"Natalia O.","full_name":"Dranenko, Natalia O.","last_name":"Dranenko"},{"first_name":"Elena S.","full_name":"Ocheredko, Elena S.","last_name":"Ocheredko"},{"full_name":"Kanevsky, German M.","last_name":"Kanevsky","first_name":"German M."},{"full_name":"Lozinsky, Yaroslav N.","last_name":"Lozinsky","first_name":"Yaroslav N."},{"first_name":"Vera A.","full_name":"Khalaycheva, Vera A.","last_name":"Khalaycheva"},{"full_name":"Artamonova, Irena I.","last_name":"Artamonova","first_name":"Irena I."},{"first_name":"Mikhail S.","full_name":"Gelfand, Mikhail S.","last_name":"Gelfand"}]},{"author":[{"full_name":"Carvalho, Maria Isabel","last_name":"Carvalho","first_name":"Maria Isabel"},{"first_name":"Rodolfo","full_name":"Bianchini, Rodolfo","last_name":"Bianchini"},{"orcid":"0000-0002-8777-3502","full_name":"Fazekas-Singer, Judit","last_name":"Fazekas-Singer","id":"36432834-F248-11E8-B48F-1D18A9856A87","first_name":"Judit"},{"first_name":"Ina","full_name":"Herrmann, Ina","last_name":"Herrmann"},{"last_name":"Flickinger","full_name":"Flickinger, Irene","first_name":"Irene"},{"last_name":"Thalhammer","full_name":"Thalhammer, Johann G.","first_name":"Johann G."},{"first_name":"Isabel","last_name":"Pires","full_name":"Pires, Isabel"},{"full_name":"Jensen-Jarolim, Erika","last_name":"Jensen-Jarolim","first_name":"Erika"},{"first_name":"Felisbina L.","full_name":"Queiroga, Felisbina L.","last_name":"Queiroga"}],"publication_identifier":{"eissn":["1791-7530"],"issn":["0250-7005"]},"publication":"Anticancer Research","page":"2811-2817","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","day":"01","language":[{"iso":"eng"}],"month":"05","year":"2018","doi":"10.21873/anticanres.12525","date_published":"2018-05-01T00:00:00Z","intvolume":"        38","date_updated":"2021-01-12T08:17:52Z","_id":"8274","citation":{"ista":"Carvalho MI, Bianchini R, Singer J, Herrmann I, Flickinger I, Thalhammer JG, Pires I, Jensen-Jarolim E, Queiroga FL. 2018. Bidirectional regulation of COX-2 expression between cancer cells and macrophages. Anticancer Research. 38(5), 2811–2817.","ieee":"M. I. Carvalho <i>et al.</i>, “Bidirectional regulation of COX-2 expression between cancer cells and macrophages,” <i>Anticancer Research</i>, vol. 38, no. 5. International Institute of Anticancer Research, pp. 2811–2817, 2018.","apa":"Carvalho, M. I., Bianchini, R., Singer, J., Herrmann, I., Flickinger, I., Thalhammer, J. G., … Queiroga, F. L. (2018). Bidirectional regulation of COX-2 expression between cancer cells and macrophages. <i>Anticancer Research</i>. International Institute of Anticancer Research. <a href=\"https://doi.org/10.21873/anticanres.12525\">https://doi.org/10.21873/anticanres.12525</a>","ama":"Carvalho MI, Bianchini R, Singer J, et al. Bidirectional regulation of COX-2 expression between cancer cells and macrophages. <i>Anticancer Research</i>. 2018;38(5):2811-2817. doi:<a href=\"https://doi.org/10.21873/anticanres.12525\">10.21873/anticanres.12525</a>","short":"M.I. Carvalho, R. Bianchini, J. Singer, I. Herrmann, I. Flickinger, J.G. Thalhammer, I. Pires, E. Jensen-Jarolim, F.L. Queiroga, Anticancer Research 38 (2018) 2811–2817.","chicago":"Carvalho, Maria Isabel, Rodolfo Bianchini, Judit Singer, Ina Herrmann, Irene Flickinger, Johann G. Thalhammer, Isabel Pires, Erika Jensen-Jarolim, and Felisbina L. Queiroga. “Bidirectional Regulation of COX-2 Expression between Cancer Cells and Macrophages.” <i>Anticancer Research</i>. International Institute of Anticancer Research, 2018. <a href=\"https://doi.org/10.21873/anticanres.12525\">https://doi.org/10.21873/anticanres.12525</a>.","mla":"Carvalho, Maria Isabel, et al. “Bidirectional Regulation of COX-2 Expression between Cancer Cells and Macrophages.” <i>Anticancer Research</i>, vol. 38, no. 5, International Institute of Anticancer Research, 2018, pp. 2811–17, doi:<a href=\"https://doi.org/10.21873/anticanres.12525\">10.21873/anticanres.12525</a>."},"publisher":"International Institute of Anticancer Research","abstract":[{"text":"Background/Aim: Our aim was to investigate the crosstalk between tumor and immune cells (M2 macrophages) and its effects on cyclo-oxygenase-2 (COX2) regulation in canine mammary tumors (CMT). Materials and Methods: Sh1b CMT cells and human BT474 mammary or HT29 colon cancer cells were co-cultured with canine peripheral blood mononuclear cells (PBMCs) or with macrophage-like differentiated THP1 monocytes (dTHP1). Intracellular COX2 expression by PBMCs, dTHP1 and cancer cells was evaluated by flow cytometry. Results: Co-culturing of Sh1b and canine PBMCs induced COX2 overexpression in CMT cells. In turn, COX2 expression by PBMCs, mostly CD68+ macrophages, was attenuated by co-culture with Sh1b (p=0.0001). In accordance, co-culture with dTHP1 prompted intracellular production of COX2 in both Sh1b CMT cells and HT29 human colon cancer cells and reduced production of COX2 in BT474 human mammary cancer cells. The intracellular COX2 expression from dTHP1 decreased when treated with conditioned medium from cultured Sh1b and HT29 cancer cells. Conclusion: Bidirectional COX2 regulation between cancer and monocytes/macrophages might shape a tolerogenic tumor microenvironment in CMT.","lang":"eng"}],"date_created":"2020-08-17T07:13:55Z","quality_controlled":"1","volume":38,"publication_status":"published","status":"public","oa_version":"None","type":"journal_article","article_type":"original","extern":"1","issue":"5","article_processing_charge":"No","title":"Bidirectional regulation of COX-2 expression between cancer cells and macrophages"},{"month":"07","language":[{"iso":"eng"}],"day":"26","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","page":"583-598","publication":"2018 IEEE Symposium on Security and Privacy","publication_identifier":{"issn":["2375-1207"],"isbn":["9781538643532"]},"author":[{"full_name":"Kokoris Kogias, Eleftherios","last_name":"Kokoris Kogias","id":"f5983044-d7ef-11ea-ac6d-fd1430a26d30","first_name":"Eleftherios"},{"first_name":"Philipp","full_name":"Jovanovic, Philipp","last_name":"Jovanovic"},{"last_name":"Gasser","full_name":"Gasser, Linus","first_name":"Linus"},{"last_name":"Gailly","full_name":"Gailly, Nicolas","first_name":"Nicolas"},{"full_name":"Syta, Ewa","last_name":"Syta","first_name":"Ewa"},{"full_name":"Ford, Bryan","last_name":"Ford","first_name":"Bryan"}],"date_updated":"2021-01-12T08:17:56Z","date_published":"2018-07-26T00:00:00Z","doi":"10.1109/sp.2018.000-5","year":"2018","main_file_link":[{"url":"https://eprint.iacr.org/2017/406","open_access":"1"}],"quality_controlled":"1","date_created":"2020-08-26T11:46:35Z","abstract":[{"lang":"eng","text":"Designing a secure permissionless distributed ledger (blockchain) that performs on par with centralized payment\r\nprocessors, such as Visa, is a challenging task. Most existing distributed ledgers are unable to scale-out, i.e., to grow their totalprocessing capacity with the number of validators; and those that do, compromise security or decentralization. We present OmniLedger, a novel scale-out distributed ledger that preserves longterm security under permissionless operation. It ensures security and correctness by using a bias-resistant public-randomness protocol for choosing large, statistically representative shards that process transactions, and by introducing an efficient crossshard commit protocol that atomically handles transactions affecting multiple shards. OmniLedger also optimizes performance via parallel intra-shard transaction processing, ledger pruning via collectively-signed state blocks, and low-latency “trust-butverify” \r\nvalidation for low-value transactions. An evaluation ofour experimental prototype shows that OmniLedger’s throughput\r\nscales linearly in the number of active validators, supporting Visa-level workloads and beyond, while confirming typical transactions in under two seconds."}],"publisher":"IEEE","citation":{"ieee":"E. Kokoris Kogias, P. Jovanovic, L. Gasser, N. Gailly, E. Syta, and B. Ford, “OmniLedger: A secure, scale-out, decentralized ledger via sharding,” in <i>2018 IEEE Symposium on Security and Privacy</i>, San Francisco, CA, United States, 2018, pp. 583–598.","ista":"Kokoris Kogias E, Jovanovic P, Gasser L, Gailly N, Syta E, Ford B. 2018. OmniLedger: A secure, scale-out, decentralized ledger via sharding. 2018 IEEE Symposium on Security and Privacy. SP: Symposium on Security and Privacy, 583–598.","ama":"Kokoris Kogias E, Jovanovic P, Gasser L, Gailly N, Syta E, Ford B. OmniLedger: A secure, scale-out, decentralized ledger via sharding. In: <i>2018 IEEE Symposium on Security and Privacy</i>. IEEE; 2018:583-598. doi:<a href=\"https://doi.org/10.1109/sp.2018.000-5\">10.1109/sp.2018.000-5</a>","apa":"Kokoris Kogias, E., Jovanovic, P., Gasser, L., Gailly, N., Syta, E., &#38; Ford, B. (2018). OmniLedger: A secure, scale-out, decentralized ledger via sharding. In <i>2018 IEEE Symposium on Security and Privacy</i> (pp. 583–598). San Francisco, CA, United States: IEEE. <a href=\"https://doi.org/10.1109/sp.2018.000-5\">https://doi.org/10.1109/sp.2018.000-5</a>","short":"E. Kokoris Kogias, P. Jovanovic, L. Gasser, N. Gailly, E. Syta, B. Ford, in:, 2018 IEEE Symposium on Security and Privacy, IEEE, 2018, pp. 583–598.","chicago":"Kokoris Kogias, Eleftherios, Philipp Jovanovic, Linus Gasser, Nicolas Gailly, Ewa Syta, and Bryan Ford. “OmniLedger: A Secure, Scale-out, Decentralized Ledger via Sharding.” In <i>2018 IEEE Symposium on Security and Privacy</i>, 583–98. IEEE, 2018. <a href=\"https://doi.org/10.1109/sp.2018.000-5\">https://doi.org/10.1109/sp.2018.000-5</a>.","mla":"Kokoris Kogias, Eleftherios, et al. “OmniLedger: A Secure, Scale-out, Decentralized Ledger via Sharding.” <i>2018 IEEE Symposium on Security and Privacy</i>, IEEE, 2018, pp. 583–98, doi:<a href=\"https://doi.org/10.1109/sp.2018.000-5\">10.1109/sp.2018.000-5</a>."},"_id":"8297","oa":1,"title":"OmniLedger: A secure, scale-out, decentralized ledger via sharding","article_processing_charge":"No","extern":"1","conference":{"start_date":"2018-05-20","location":"San Francisco, CA, United States","end_date":"2018-05-24","name":"SP: Symposium on Security and Privacy"},"oa_version":"Preprint","type":"conference","publication_status":"published","status":"public"},{"type":"conference","oa_version":"None","status":"public","publication_status":"published","title":"Channels: Horizontal scaling and confidentiality on permissioned blockchains","article_processing_charge":"No","extern":"1","conference":{"end_date":"2018-09-07","name":"ESORICS: European Symposium on Research in Computer Security","start_date":"2018-09-03","location":"Barcelona, Spain"},"publisher":"Springer Nature","citation":{"chicago":"Androulaki, Elli, Christian Cachin, Angelo De Caro, and Eleftherios Kokoris Kogias. “Channels: Horizontal Scaling and Confidentiality on Permissioned Blockchains.” In <i>Computer Security</i>, 11098:111–31. Springer Nature, 2018. <a href=\"https://doi.org/10.1007/978-3-319-99073-6_6\">https://doi.org/10.1007/978-3-319-99073-6_6</a>.","mla":"Androulaki, Elli, et al. “Channels: Horizontal Scaling and Confidentiality on Permissioned Blockchains.” <i>Computer Security</i>, vol. 11098, Springer Nature, 2018, pp. 111–31, doi:<a href=\"https://doi.org/10.1007/978-3-319-99073-6_6\">10.1007/978-3-319-99073-6_6</a>.","short":"E. Androulaki, C. Cachin, A. De Caro, E. Kokoris Kogias, in:, Computer Security, Springer Nature, 2018, pp. 111–131.","apa":"Androulaki, E., Cachin, C., De Caro, A., &#38; Kokoris Kogias, E. (2018). Channels: Horizontal scaling and confidentiality on permissioned blockchains. In <i>Computer Security</i> (Vol. 11098, pp. 111–131). Barcelona, Spain: Springer Nature. <a href=\"https://doi.org/10.1007/978-3-319-99073-6_6\">https://doi.org/10.1007/978-3-319-99073-6_6</a>","ama":"Androulaki E, Cachin C, De Caro A, Kokoris Kogias E. Channels: Horizontal scaling and confidentiality on permissioned blockchains. In: <i>Computer Security</i>. Vol 11098. Springer Nature; 2018:111-131. doi:<a href=\"https://doi.org/10.1007/978-3-319-99073-6_6\">10.1007/978-3-319-99073-6_6</a>","ista":"Androulaki E, Cachin C, De Caro A, Kokoris Kogias E. 2018. Channels: Horizontal scaling and confidentiality on permissioned blockchains. Computer Security. ESORICS: European Symposium on Research in Computer Security, LNCS, vol. 11098, 111–131.","ieee":"E. Androulaki, C. Cachin, A. De Caro, and E. Kokoris Kogias, “Channels: Horizontal scaling and confidentiality on permissioned blockchains,” in <i>Computer Security</i>, Barcelona, Spain, 2018, vol. 11098, pp. 111–131."},"_id":"8298","quality_controlled":"1","volume":11098,"date_created":"2020-08-26T11:47:34Z","abstract":[{"text":"Sharding, or partitioning the system’s state so that different subsets of participants handle it, is a proven approach to building distributed systems whose total capacity scales horizontally with the number of participants. Many distributed ledgers have adopted this approach to increase their performance, however, they focus on the permissionless setting that assumes the existence of a strong adversary. In this paper, we deploy channels for permissioned blockchains. Our first contribution is to adapt sharding on asset-management applications for the permissioned setting, while preserving liveness and safety even on transactions spanning across-channels. Our second contribution is to leverage channels as a confidentiality boundary, enabling different organizations and consortia to preserve their privacy within their channels and still be part of a bigger collaborative ecosystem. To make our system concrete we map it on top of Hyperledger Fabric.","lang":"eng"}],"alternative_title":["LNCS"],"year":"2018","date_updated":"2021-01-12T08:17:57Z","intvolume":"     11098","date_published":"2018-08-08T00:00:00Z","doi":"10.1007/978-3-319-99073-6_6","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Computer Security","page":"111-131","publication_identifier":{"isbn":["9783319990729"],"eisbn":["9783319990736"],"issn":["0302-9743","1611-3349"]},"author":[{"last_name":"Androulaki","full_name":"Androulaki, Elli","first_name":"Elli"},{"first_name":"Christian","last_name":"Cachin","full_name":"Cachin, Christian"},{"first_name":"Angelo","full_name":"De Caro, Angelo","last_name":"De Caro"},{"id":"f5983044-d7ef-11ea-ac6d-fd1430a26d30","first_name":"Eleftherios","full_name":"Kokoris Kogias, Eleftherios","last_name":"Kokoris Kogias"}],"month":"08","language":[{"iso":"eng"}],"day":"08"},{"related_material":{"record":[{"relation":"part_of_dissertation","status":"public","id":"1229"},{"id":"1235","relation":"part_of_dissertation","status":"public"},{"id":"1236","status":"public","relation":"part_of_dissertation"},{"status":"public","relation":"part_of_dissertation","id":"559"}]},"date_published":"2018-09-05T00:00:00Z","pubrep_id":"1046","has_accepted_license":"1","alternative_title":["ISTA Thesis"],"ddc":["004"],"day":"05","language":[{"iso":"eng"}],"publication_identifier":{"issn":["2663-337X"]},"publist_id":"7971","supervisor":[{"last_name":"Pietrzak","orcid":"0000-0002-9139-1654","full_name":"Pietrzak, Krzysztof Z","first_name":"Krzysztof Z","id":"3E04A7AA-F248-11E8-B48F-1D18A9856A87"}],"degree_awarded":"PhD","oa_version":"Published Version","type":"dissertation","abstract":[{"lang":"eng","text":"A proof system is a protocol between a prover and a verifier over a common input in which an honest prover convinces the verifier of the validity of true statements. Motivated by the success of decentralized cryptocurrencies, exemplified by Bitcoin, the focus of this thesis will be on proof systems which found applications in some sustainable alternatives to Bitcoin, such as the Spacemint and Chia cryptocurrencies. In particular, we focus on proofs of space and proofs of sequential work.\r\nProofs of space (PoSpace) were suggested as more ecological, economical, and egalitarian alternative to the energy-wasteful proof-of-work mining of Bitcoin. However, the state-of-the-art constructions of PoSpace are based on sophisticated graph pebbling lower bounds, and are therefore complex. Moreover, when these PoSpace are used in cryptocurrencies like Spacemint, miners can only start mining after ensuring that a commitment to their space is already added in a special transaction to the blockchain. Proofs of sequential work (PoSW) are proof systems in which a prover, upon receiving a statement x and a time parameter T, computes a proof which convinces the verifier that T time units had passed since x was received. Whereas Spacemint assumes synchrony to retain some interesting Bitcoin dynamics, Chia requires PoSW with unique proofs, i.e., PoSW in which it is hard to come up with more than one accepting proof for any true statement. In this thesis we construct simple and practically-efficient PoSpace and PoSW. When using our PoSpace in cryptocurrencies, miners can start mining on the fly, like in Bitcoin, and unlike current constructions of PoSW, which either achieve efficient verification of sequential work, or faster-than-recomputing verification of correctness of proofs, but not both at the same time, ours achieve the best of these two worlds."}],"_id":"83","project":[{"grant_number":"259668","name":"Provable Security for Physical Cryptography","_id":"258C570E-B435-11E9-9278-68D0E5697425","call_identifier":"FP7"},{"call_identifier":"H2020","_id":"258AA5B2-B435-11E9-9278-68D0E5697425","name":"Teaching Old Crypto New Tricks","grant_number":"682815"}],"doi":"10.15479/AT:ISTA:TH_1046","date_updated":"2023-09-07T12:30:23Z","year":"2018","month":"09","department":[{"_id":"KrPi"}],"author":[{"id":"40297222-F248-11E8-B48F-1D18A9856A87","first_name":"Hamza M","last_name":"Abusalah","full_name":"Abusalah, Hamza M"}],"user_id":"c635000d-4b10-11ee-a964-aac5a93f6ac1","page":"59","title":"Proof systems for sustainable decentralized cryptocurrencies","article_processing_charge":"No","publication_status":"published","status":"public","ec_funded":1,"file_date_updated":"2020-07-14T12:48:11Z","date_created":"2018-12-11T11:44:32Z","file":[{"date_updated":"2020-07-14T12:48:11Z","relation":"main_file","checksum":"c4b5f7d111755d1396787f41886fc674","content_type":"application/pdf","date_created":"2019-04-09T06:43:41Z","creator":"dernst","file_name":"2018_Thesis_Abusalah.pdf","file_id":"6245","file_size":876241,"access_level":"open_access"},{"relation":"source_file","content_type":"application/x-gzip","checksum":"0f382ac56b471c48fd907d63eb87dafe","date_updated":"2020-07-14T12:48:11Z","access_level":"closed","file_size":2029190,"file_name":"2018_Thesis_Abusalah_source.tar.gz","file_id":"6246","creator":"dernst","date_created":"2019-04-09T06:43:41Z"}],"publisher":"Institute of Science and Technology Austria","citation":{"ieee":"H. M. Abusalah, “Proof systems for sustainable decentralized cryptocurrencies,” Institute of Science and Technology Austria, 2018.","ista":"Abusalah HM. 2018. Proof systems for sustainable decentralized cryptocurrencies. Institute of Science and Technology Austria.","ama":"Abusalah HM. Proof systems for sustainable decentralized cryptocurrencies. 2018. doi:<a href=\"https://doi.org/10.15479/AT:ISTA:TH_1046\">10.15479/AT:ISTA:TH_1046</a>","apa":"Abusalah, H. M. (2018). <i>Proof systems for sustainable decentralized cryptocurrencies</i>. Institute of Science and Technology Austria. <a href=\"https://doi.org/10.15479/AT:ISTA:TH_1046\">https://doi.org/10.15479/AT:ISTA:TH_1046</a>","short":"H.M. Abusalah, Proof Systems for Sustainable Decentralized Cryptocurrencies, Institute of Science and Technology Austria, 2018.","mla":"Abusalah, Hamza M. <i>Proof Systems for Sustainable Decentralized Cryptocurrencies</i>. Institute of Science and Technology Austria, 2018, doi:<a href=\"https://doi.org/10.15479/AT:ISTA:TH_1046\">10.15479/AT:ISTA:TH_1046</a>.","chicago":"Abusalah, Hamza M. “Proof Systems for Sustainable Decentralized Cryptocurrencies.” Institute of Science and Technology Austria, 2018. <a href=\"https://doi.org/10.15479/AT:ISTA:TH_1046\">https://doi.org/10.15479/AT:ISTA:TH_1046</a>."},"oa":1},{"type":"journal_article","oa_version":"None","status":"public","publication_status":"published","issue":"3","article_processing_charge":"No","title":"Global instability in the restricted planar elliptic three body problem","article_type":"original","extern":"1","keyword":["Mathematical Physics","Statistical and Nonlinear Physics"],"citation":{"ista":"Delshams A, Kaloshin V, de la Rosa A, Seara TM. 2018. Global instability in the restricted planar elliptic three body problem. Communications in Mathematical Physics. 366(3), 1173–1228.","ieee":"A. Delshams, V. Kaloshin, A. de la Rosa, and T. M. Seara, “Global instability in the restricted planar elliptic three body problem,” <i>Communications in Mathematical Physics</i>, vol. 366, no. 3. Springer Nature, pp. 1173–1228, 2018.","apa":"Delshams, A., Kaloshin, V., de la Rosa, A., &#38; Seara, T. M. (2018). Global instability in the restricted planar elliptic three body problem. <i>Communications in Mathematical Physics</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s00220-018-3248-z\">https://doi.org/10.1007/s00220-018-3248-z</a>","ama":"Delshams A, Kaloshin V, de la Rosa A, Seara TM. Global instability in the restricted planar elliptic three body problem. <i>Communications in Mathematical Physics</i>. 2018;366(3):1173-1228. doi:<a href=\"https://doi.org/10.1007/s00220-018-3248-z\">10.1007/s00220-018-3248-z</a>","short":"A. Delshams, V. Kaloshin, A. de la Rosa, T.M. Seara, Communications in Mathematical Physics 366 (2018) 1173–1228.","mla":"Delshams, Amadeu, et al. “Global Instability in the Restricted Planar Elliptic Three Body Problem.” <i>Communications in Mathematical Physics</i>, vol. 366, no. 3, Springer Nature, 2018, pp. 1173–228, doi:<a href=\"https://doi.org/10.1007/s00220-018-3248-z\">10.1007/s00220-018-3248-z</a>.","chicago":"Delshams, Amadeu, Vadim Kaloshin, Abraham de la Rosa, and Tere M. Seara. “Global Instability in the Restricted Planar Elliptic Three Body Problem.” <i>Communications in Mathematical Physics</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1007/s00220-018-3248-z\">https://doi.org/10.1007/s00220-018-3248-z</a>."},"_id":"8417","publisher":"Springer Nature","date_created":"2020-09-17T10:41:43Z","quality_controlled":"1","volume":366,"abstract":[{"lang":"eng","text":"The restricted planar elliptic three body problem (RPETBP) describes the motion of a massless particle (a comet or an asteroid) under the gravitational field of two massive bodies (the primaries, say the Sun and Jupiter) revolving around their center of mass on elliptic orbits with some positive eccentricity. The aim of this paper is to show the existence of orbits whose angular momentum performs arbitrary excursions in a large region. In particular, there exist diffusive orbits, that is, with a large variation of angular momentum. The leading idea of the proof consists in analyzing parabolic motions of the comet. By a well-known result of McGehee, the union of future (resp. past) parabolic orbits is an analytic manifold P+ (resp. P−). In a properly chosen coordinate system these manifolds are stable (resp. unstable) manifolds of a manifold at infinity P∞, which we call the manifold at parabolic infinity. On P∞ it is possible to define two scattering maps, which contain the map structure of the homoclinic trajectories to it, i.e. orbits parabolic both in the future and the past. Since the inner dynamics inside P∞ is trivial, two different scattering maps are used. The combination of these two scattering maps permits the design of the desired diffusive pseudo-orbits. Using shadowing techniques and these pseudo orbits we show the existence of true trajectories of the RPETBP whose angular momentum varies in any predetermined fashion."}],"year":"2018","intvolume":"       366","date_updated":"2021-01-12T08:19:08Z","date_published":"2018-09-05T00:00:00Z","doi":"10.1007/s00220-018-3248-z","page":"1173-1228","publication":"Communications in Mathematical Physics","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"first_name":"Amadeu","full_name":"Delshams, Amadeu","last_name":"Delshams"},{"last_name":"Kaloshin","orcid":"0000-0002-6051-2628","full_name":"Kaloshin, Vadim","id":"FE553552-CDE8-11E9-B324-C0EBE5697425","first_name":"Vadim"},{"last_name":"de la Rosa","full_name":"de la Rosa, Abraham","first_name":"Abraham"},{"first_name":"Tere M.","last_name":"Seara","full_name":"Seara, Tere M."}],"publication_identifier":{"issn":["0010-3616","1432-0916"]},"month":"09","day":"05","language":[{"iso":"eng"}]},{"year":"2018","intvolume":"       376","date_updated":"2021-01-12T08:19:09Z","doi":"10.1098/rsta.2017.0419","date_published":"2018-10-28T00:00:00Z","publication":"Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences","article_number":"20170419","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"first_name":"Vadim","id":"FE553552-CDE8-11E9-B324-C0EBE5697425","last_name":"Kaloshin","full_name":"Kaloshin, Vadim","orcid":"0000-0002-6051-2628"},{"last_name":"Sorrentino","full_name":"Sorrentino, Alfonso","first_name":"Alfonso"}],"publication_identifier":{"issn":["1364-503X","1471-2962"]},"month":"10","day":"28","language":[{"iso":"eng"}],"oa_version":"None","type":"journal_article","publication_status":"published","status":"public","article_processing_charge":"No","issue":"2131","title":"On the integrability of Birkhoff billiards","article_type":"original","extern":"1","keyword":["General Engineering","General Physics and Astronomy","General Mathematics"],"_id":"8419","citation":{"chicago":"Kaloshin, Vadim, and Alfonso Sorrentino. “On the Integrability of Birkhoff Billiards.” <i>Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences</i>. The Royal Society, 2018. <a href=\"https://doi.org/10.1098/rsta.2017.0419\">https://doi.org/10.1098/rsta.2017.0419</a>.","mla":"Kaloshin, Vadim, and Alfonso Sorrentino. “On the Integrability of Birkhoff Billiards.” <i>Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences</i>, vol. 376, no. 2131, 20170419, The Royal Society, 2018, doi:<a href=\"https://doi.org/10.1098/rsta.2017.0419\">10.1098/rsta.2017.0419</a>.","short":"V. Kaloshin, A. Sorrentino, Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences 376 (2018).","apa":"Kaloshin, V., &#38; Sorrentino, A. (2018). On the integrability of Birkhoff billiards. <i>Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences</i>. The Royal Society. <a href=\"https://doi.org/10.1098/rsta.2017.0419\">https://doi.org/10.1098/rsta.2017.0419</a>","ama":"Kaloshin V, Sorrentino A. On the integrability of Birkhoff billiards. <i>Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences</i>. 2018;376(2131). doi:<a href=\"https://doi.org/10.1098/rsta.2017.0419\">10.1098/rsta.2017.0419</a>","ista":"Kaloshin V, Sorrentino A. 2018. On the integrability of Birkhoff billiards. Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences. 376(2131), 20170419.","ieee":"V. Kaloshin and A. Sorrentino, “On the integrability of Birkhoff billiards,” <i>Philosophical Transactions of the Royal Society A: Mathematical, Physical and Engineering Sciences</i>, vol. 376, no. 2131. The Royal Society, 2018."},"publisher":"The Royal Society","date_created":"2020-09-17T10:42:01Z","quality_controlled":"1","volume":376,"abstract":[{"lang":"eng","text":"In this survey, we provide a concise introduction to convex billiards and describe some recent results, obtained by the authors and collaborators, on the classification of integrable billiards, namely the so-called Birkhoff conjecture.\r\n\r\nThis article is part of the theme issue ‘Finite dimensional integrable systems: new trends and methods’."}]},{"day":"15","language":[{"iso":"eng"}],"arxiv":1,"publication_identifier":{"issn":["0951-7715","1361-6544"]},"publication":"Nonlinearity","date_published":"2018-10-15T00:00:00Z","intvolume":"        31","abstract":[{"text":"We show that in the space of all convex billiard boundaries, the set of boundaries with rational caustics is dense. More precisely, the set of billiard boundaries with caustics of rotation number 1/q is polynomially sense in the smooth case, and exponentially dense in the analytic case.","lang":"eng"}],"volume":31,"_id":"8420","issue":"11","type":"journal_article","oa_version":"Preprint","month":"10","author":[{"first_name":"Vadim","id":"FE553552-CDE8-11E9-B324-C0EBE5697425","last_name":"Kaloshin","full_name":"Kaloshin, Vadim","orcid":"0000-0002-6051-2628"},{"full_name":"Zhang, Ke","last_name":"Zhang","first_name":"Ke"}],"page":"5214-5234","external_id":{"arxiv":["1706.07968"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","doi":"10.1088/1361-6544/aadc12","date_updated":"2021-01-12T08:19:10Z","year":"2018","date_created":"2020-09-17T10:42:09Z","main_file_link":[{"url":"https://arxiv.org/abs/1706.07968","open_access":"1"}],"quality_controlled":"1","oa":1,"citation":{"mla":"Kaloshin, Vadim, and Ke Zhang. “Density of Convex Billiards with Rational Caustics.” <i>Nonlinearity</i>, vol. 31, no. 11, IOP Publishing, 2018, pp. 5214–34, doi:<a href=\"https://doi.org/10.1088/1361-6544/aadc12\">10.1088/1361-6544/aadc12</a>.","chicago":"Kaloshin, Vadim, and Ke Zhang. “Density of Convex Billiards with Rational Caustics.” <i>Nonlinearity</i>. IOP Publishing, 2018. <a href=\"https://doi.org/10.1088/1361-6544/aadc12\">https://doi.org/10.1088/1361-6544/aadc12</a>.","short":"V. Kaloshin, K. Zhang, Nonlinearity 31 (2018) 5214–5234.","apa":"Kaloshin, V., &#38; Zhang, K. (2018). Density of convex billiards with rational caustics. <i>Nonlinearity</i>. IOP Publishing. <a href=\"https://doi.org/10.1088/1361-6544/aadc12\">https://doi.org/10.1088/1361-6544/aadc12</a>","ama":"Kaloshin V, Zhang K. Density of convex billiards with rational caustics. <i>Nonlinearity</i>. 2018;31(11):5214-5234. doi:<a href=\"https://doi.org/10.1088/1361-6544/aadc12\">10.1088/1361-6544/aadc12</a>","ista":"Kaloshin V, Zhang K. 2018. Density of convex billiards with rational caustics. Nonlinearity. 31(11), 5214–5234.","ieee":"V. Kaloshin and K. Zhang, “Density of convex billiards with rational caustics,” <i>Nonlinearity</i>, vol. 31, no. 11. IOP Publishing, pp. 5214–5234, 2018."},"publisher":"IOP Publishing","keyword":["Mathematical Physics","General Physics and Astronomy","Applied Mathematics","Statistical and Nonlinear Physics"],"article_type":"original","extern":"1","article_processing_charge":"No","title":"Density of convex billiards with rational caustics","publication_status":"published","status":"public"},{"page":"315-380","external_id":{"arxiv":["1612.09194"]},"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"id":"FE553552-CDE8-11E9-B324-C0EBE5697425","first_name":"Vadim","last_name":"Kaloshin","full_name":"Kaloshin, Vadim","orcid":"0000-0002-6051-2628"},{"first_name":"Alfonso","full_name":"Sorrentino, Alfonso","last_name":"Sorrentino"}],"month":"07","year":"2018","date_updated":"2021-01-12T08:19:10Z","doi":"10.4007/annals.2018.188.1.6","keyword":["Statistics","Probability and Uncertainty","Statistics and Probability"],"oa":1,"citation":{"ama":"Kaloshin V, Sorrentino A. On the local Birkhoff conjecture for convex billiards. <i>Annals of Mathematics</i>. 2018;188(1):315-380. doi:<a href=\"https://doi.org/10.4007/annals.2018.188.1.6\">10.4007/annals.2018.188.1.6</a>","apa":"Kaloshin, V., &#38; Sorrentino, A. (2018). On the local Birkhoff conjecture for convex billiards. <i>Annals of Mathematics</i>. Annals of Mathematics, Princeton U. <a href=\"https://doi.org/10.4007/annals.2018.188.1.6\">https://doi.org/10.4007/annals.2018.188.1.6</a>","ieee":"V. Kaloshin and A. Sorrentino, “On the local Birkhoff conjecture for convex billiards,” <i>Annals of Mathematics</i>, vol. 188, no. 1. Annals of Mathematics, Princeton U, pp. 315–380, 2018.","ista":"Kaloshin V, Sorrentino A. 2018. On the local Birkhoff conjecture for convex billiards. Annals of Mathematics. 188(1), 315–380.","chicago":"Kaloshin, Vadim, and Alfonso Sorrentino. “On the Local Birkhoff Conjecture for Convex Billiards.” <i>Annals of Mathematics</i>. Annals of Mathematics, Princeton U, 2018. <a href=\"https://doi.org/10.4007/annals.2018.188.1.6\">https://doi.org/10.4007/annals.2018.188.1.6</a>.","mla":"Kaloshin, Vadim, and Alfonso Sorrentino. “On the Local Birkhoff Conjecture for Convex Billiards.” <i>Annals of Mathematics</i>, vol. 188, no. 1, Annals of Mathematics, Princeton U, 2018, pp. 315–80, doi:<a href=\"https://doi.org/10.4007/annals.2018.188.1.6\">10.4007/annals.2018.188.1.6</a>.","short":"V. Kaloshin, A. Sorrentino, Annals of Mathematics 188 (2018) 315–380."},"publisher":"Annals of Mathematics, Princeton U","date_created":"2020-09-17T10:42:22Z","main_file_link":[{"open_access":"1","url":"https://arxiv.org/abs/1612.09194"}],"quality_controlled":"1","status":"public","publication_status":"published","article_processing_charge":"No","title":"On the local Birkhoff conjecture for convex billiards","article_type":"original","extern":"1","publication":"Annals of Mathematics","arxiv":1,"publication_identifier":{"issn":["0003-486X"]},"language":[{"iso":"eng"}],"day":"01","intvolume":"       188","date_published":"2018-07-01T00:00:00Z","_id":"8421","volume":188,"abstract":[{"text":"The classical Birkhoff conjecture claims that the boundary of a strictly convex integrable billiard table is necessarily an ellipse (or a circle as a special case). In this article we prove a complete local version of this conjecture: a small integrable perturbation of an ellipse must be an ellipse. This extends and completes the result in Avila-De Simoi-Kaloshin, where nearly circular domains were considered. One of the crucial ideas in the proof is to extend action-angle coordinates for elliptic billiards into complex domains (with respect to the angle), and to thoroughly analyze the nature of their complex singularities. As an application, we are able to prove some spectral rigidity results for elliptic domains.","lang":"eng"}],"type":"journal_article","oa_version":"Preprint","issue":"1"},{"date_published":"2018-03-18T00:00:00Z","intvolume":"        28","day":"18","language":[{"iso":"eng"}],"publication_identifier":{"issn":["1016-443X","1420-8970"]},"arxiv":1,"publication":"Geometric and Functional Analysis","issue":"2","oa_version":"Preprint","type":"journal_article","abstract":[{"lang":"eng","text":"The Birkhoff conjecture says that the boundary of a strictly convex integrable billiard table is necessarily an ellipse. In this article, we consider a stronger notion of integrability, namely integrability close to the boundary, and prove a local version of this conjecture: a small perturbation of an ellipse of small eccentricity which preserves integrability near the boundary, is itself an ellipse. This extends the result in Avila et al. (Ann Math 184:527–558, ADK16), where integrability was assumed on a larger set. In particular, it shows that (local) integrability near the boundary implies global integrability. One of the crucial ideas in the proof consists in analyzing Taylor expansion of the corresponding action-angle coordinates with respect to the eccentricity parameter, deriving and studying higher order conditions for the preservation of integrable rational caustics."}],"volume":28,"_id":"8422","doi":"10.1007/s00039-018-0440-4","date_updated":"2021-01-12T08:19:11Z","year":"2018","month":"03","author":[{"first_name":"Guan","full_name":"Huang, Guan","last_name":"Huang"},{"id":"FE553552-CDE8-11E9-B324-C0EBE5697425","first_name":"Vadim","last_name":"Kaloshin","full_name":"Kaloshin, Vadim","orcid":"0000-0002-6051-2628"},{"first_name":"Alfonso","last_name":"Sorrentino","full_name":"Sorrentino, Alfonso"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","page":"334-392","external_id":{"arxiv":["1705.10601"]},"extern":"1","article_type":"original","title":"Nearly circular domains which are integrable close to the boundary are ellipses","article_processing_charge":"No","publication_status":"published","status":"public","quality_controlled":"1","main_file_link":[{"open_access":"1","url":"https://arxiv.org/abs/1705.10601"}],"date_created":"2020-09-17T10:42:30Z","publisher":"Springer Nature","oa":1,"citation":{"short":"G. Huang, V. Kaloshin, A. Sorrentino, Geometric and Functional Analysis 28 (2018) 334–392.","mla":"Huang, Guan, et al. “Nearly Circular Domains Which Are Integrable Close to the Boundary Are Ellipses.” <i>Geometric and Functional Analysis</i>, vol. 28, no. 2, Springer Nature, 2018, pp. 334–92, doi:<a href=\"https://doi.org/10.1007/s00039-018-0440-4\">10.1007/s00039-018-0440-4</a>.","chicago":"Huang, Guan, Vadim Kaloshin, and Alfonso Sorrentino. “Nearly Circular Domains Which Are Integrable Close to the Boundary Are Ellipses.” <i>Geometric and Functional Analysis</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1007/s00039-018-0440-4\">https://doi.org/10.1007/s00039-018-0440-4</a>.","ieee":"G. Huang, V. Kaloshin, and A. Sorrentino, “Nearly circular domains which are integrable close to the boundary are ellipses,” <i>Geometric and Functional Analysis</i>, vol. 28, no. 2. Springer Nature, pp. 334–392, 2018.","ista":"Huang G, Kaloshin V, Sorrentino A. 2018. Nearly circular domains which are integrable close to the boundary are ellipses. Geometric and Functional Analysis. 28(2), 334–392.","ama":"Huang G, Kaloshin V, Sorrentino A. Nearly circular domains which are integrable close to the boundary are ellipses. <i>Geometric and Functional Analysis</i>. 2018;28(2):334-392. doi:<a href=\"https://doi.org/10.1007/s00039-018-0440-4\">10.1007/s00039-018-0440-4</a>","apa":"Huang, G., Kaloshin, V., &#38; Sorrentino, A. (2018). Nearly circular domains which are integrable close to the boundary are ellipses. <i>Geometric and Functional Analysis</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s00039-018-0440-4\">https://doi.org/10.1007/s00039-018-0440-4</a>"},"keyword":["Geometry and Topology","Analysis"]},{"intvolume":"        23","date_published":"2018-02-05T00:00:00Z","publication":"Regular and Chaotic Dynamics","publication_identifier":{"issn":["1560-3547","1468-4845"]},"arxiv":1,"language":[{"iso":"eng"}],"day":"05","oa_version":"Preprint","type":"journal_article","_id":"8426","volume":23,"abstract":[{"text":"For any strictly convex planar domain Ω ⊂ R2 with a C∞ boundary one can associate an infinite sequence of spectral invariants introduced by Marvizi–Merlose [5]. These invariants can generically be determined using the spectrum of the Dirichlet problem of the Laplace operator. A natural question asks if this collection is sufficient to determine Ω up to isometry. In this paper we give a counterexample, namely, we present two nonisometric domains Ω and Ω¯ with the same collection of Marvizi–Melrose invariants. Moreover, each domain has countably many periodic orbits {Sn}n≥1 (resp. {S¯n}n⩾1) of period going to infinity such that Sn and S¯n have the same period and perimeter for each n.","lang":"eng"}],"year":"2018","date_updated":"2021-01-12T08:19:11Z","doi":"10.1134/s1560354718010057","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","external_id":{"arxiv":["1801.00952"]},"page":"54-59","author":[{"first_name":"Lev","last_name":"Buhovsky","full_name":"Buhovsky, Lev"},{"last_name":"Kaloshin","full_name":"Kaloshin, Vadim","orcid":"0000-0002-6051-2628","id":"FE553552-CDE8-11E9-B324-C0EBE5697425","first_name":"Vadim"}],"month":"02","status":"public","publication_status":"published","title":"Nonisometric domains with the same Marvizi-Melrose invariants","article_processing_charge":"No","extern":"1","article_type":"original","publisher":"Springer Nature","oa":1,"citation":{"short":"L. Buhovsky, V. Kaloshin, Regular and Chaotic Dynamics 23 (2018) 54–59.","chicago":"Buhovsky, Lev, and Vadim Kaloshin. “Nonisometric Domains with the Same Marvizi-Melrose Invariants.” <i>Regular and Chaotic Dynamics</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1134/s1560354718010057\">https://doi.org/10.1134/s1560354718010057</a>.","mla":"Buhovsky, Lev, and Vadim Kaloshin. “Nonisometric Domains with the Same Marvizi-Melrose Invariants.” <i>Regular and Chaotic Dynamics</i>, vol. 23, Springer Nature, 2018, pp. 54–59, doi:<a href=\"https://doi.org/10.1134/s1560354718010057\">10.1134/s1560354718010057</a>.","ieee":"L. Buhovsky and V. Kaloshin, “Nonisometric domains with the same Marvizi-Melrose invariants,” <i>Regular and Chaotic Dynamics</i>, vol. 23. Springer Nature, pp. 54–59, 2018.","ista":"Buhovsky L, Kaloshin V. 2018. Nonisometric domains with the same Marvizi-Melrose invariants. Regular and Chaotic Dynamics. 23, 54–59.","ama":"Buhovsky L, Kaloshin V. Nonisometric domains with the same Marvizi-Melrose invariants. <i>Regular and Chaotic Dynamics</i>. 2018;23:54-59. doi:<a href=\"https://doi.org/10.1134/s1560354718010057\">10.1134/s1560354718010057</a>","apa":"Buhovsky, L., &#38; Kaloshin, V. (2018). Nonisometric domains with the same Marvizi-Melrose invariants. <i>Regular and Chaotic Dynamics</i>. Springer Nature. <a href=\"https://doi.org/10.1134/s1560354718010057\">https://doi.org/10.1134/s1560354718010057</a>"},"main_file_link":[{"open_access":"1","url":"https://arxiv.org/abs/1801.00952"}],"quality_controlled":"1","date_created":"2020-09-17T10:43:21Z"},{"keyword":["General Biochemistry","Genetics and Molecular Biology"],"publisher":"Elsevier","citation":{"ista":"Weinhäupl K, Lindau C, Hessel A, Wang Y, Schütze C, Jores T, Melchionda L, Schönfisch B, Kalbacher H, Bersch B, Rapaport D, Brennich M, Lindorff-Larsen K, Wiedemann N, Schanda P. 2018. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. Cell. 175(5), 1365–1379.e25.","ieee":"K. Weinhäupl <i>et al.</i>, “Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space,” <i>Cell</i>, vol. 175, no. 5. Elsevier, p. 1365–1379.e25, 2018.","apa":"Weinhäupl, K., Lindau, C., Hessel, A., Wang, Y., Schütze, C., Jores, T., … Schanda, P. (2018). Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. <i>Cell</i>. Elsevier. <a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">https://doi.org/10.1016/j.cell.2018.10.039</a>","ama":"Weinhäupl K, Lindau C, Hessel A, et al. Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space. <i>Cell</i>. 2018;175(5):1365-1379.e25. doi:<a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">10.1016/j.cell.2018.10.039</a>","short":"K. Weinhäupl, C. Lindau, A. Hessel, Y. Wang, C. Schütze, T. Jores, L. Melchionda, B. Schönfisch, H. Kalbacher, B. Bersch, D. Rapaport, M. Brennich, K. Lindorff-Larsen, N. Wiedemann, P. Schanda, Cell 175 (2018) 1365–1379.e25.","chicago":"Weinhäupl, Katharina, Caroline Lindau, Audrey Hessel, Yong Wang, Conny Schütze, Tobias Jores, Laura Melchionda, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.” <i>Cell</i>. Elsevier, 2018. <a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">https://doi.org/10.1016/j.cell.2018.10.039</a>.","mla":"Weinhäupl, Katharina, et al. “Structural Basis of Membrane Protein Chaperoning through the Mitochondrial Intermembrane Space.” <i>Cell</i>, vol. 175, no. 5, Elsevier, 2018, p. 1365–1379.e25, doi:<a href=\"https://doi.org/10.1016/j.cell.2018.10.039\">10.1016/j.cell.2018.10.039</a>."},"_id":"8436","quality_controlled":"1","volume":175,"date_created":"2020-09-18T10:04:39Z","abstract":[{"text":"The exchange of metabolites between the mitochondrial matrix and the cytosol depends on β-barrel channels in the outer membrane and α-helical carrier proteins in the inner membrane. The essential translocase of the inner membrane (TIM) chaperones escort these proteins through the intermembrane space, but the structural and mechanistic details remain elusive. We have used an integrated structural biology approach to reveal the functional principle of TIM chaperones. Multiple clamp-like binding sites hold the mitochondrial membrane proteins in a translocation-competent elongated form, thus mimicking characteristics of co-translational membrane insertion. The bound preprotein undergoes conformational dynamics within the chaperone binding clefts, pointing to a multitude of dynamic local binding events. Mutations in these binding sites cause cell death or growth defects associated with impairment of carrier and β-barrel protein biogenesis. Our work reveals how a single mitochondrial “transfer-chaperone” system is able to guide α-helical and β-barrel membrane proteins in a “nascent chain-like” conformation through a ribosome-free compartment.","lang":"eng"}],"type":"journal_article","oa_version":"None","publication_status":"published","status":"public","title":"Structural basis of membrane protein chaperoning through the mitochondrial intermembrane space","issue":"5","article_processing_charge":"No","extern":"1","article_type":"original","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","publication":"Cell","page":"1365-1379.e25","publication_identifier":{"issn":["0092-8674"]},"author":[{"last_name":"Weinhäupl","full_name":"Weinhäupl, Katharina","first_name":"Katharina"},{"first_name":"Caroline","last_name":"Lindau","full_name":"Lindau, Caroline"},{"full_name":"Hessel, Audrey","last_name":"Hessel","first_name":"Audrey"},{"first_name":"Yong","full_name":"Wang, Yong","last_name":"Wang"},{"first_name":"Conny","last_name":"Schütze","full_name":"Schütze, Conny"},{"full_name":"Jores, Tobias","last_name":"Jores","first_name":"Tobias"},{"first_name":"Laura","last_name":"Melchionda","full_name":"Melchionda, Laura"},{"full_name":"Schönfisch, Birgit","last_name":"Schönfisch","first_name":"Birgit"},{"first_name":"Hubert","full_name":"Kalbacher, Hubert","last_name":"Kalbacher"},{"last_name":"Bersch","full_name":"Bersch, Beate","first_name":"Beate"},{"full_name":"Rapaport, Doron","last_name":"Rapaport","first_name":"Doron"},{"full_name":"Brennich, Martha","last_name":"Brennich","first_name":"Martha"},{"first_name":"Kresten","last_name":"Lindorff-Larsen","full_name":"Lindorff-Larsen, Kresten"},{"first_name":"Nils","last_name":"Wiedemann","full_name":"Wiedemann, Nils"},{"last_name":"Schanda","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"month":"11","day":"15","language":[{"iso":"eng"}],"year":"2018","date_updated":"2021-01-12T08:19:15Z","intvolume":"       175","doi":"10.1016/j.cell.2018.10.039","date_published":"2018-11-15T00:00:00Z"},{"publication_identifier":{"issn":["2375-2548"]},"author":[{"first_name":"Guillaume","last_name":"Mas","full_name":"Mas, Guillaume"},{"first_name":"Jia-Ying","full_name":"Guan, Jia-Ying","last_name":"Guan"},{"first_name":"Elodie","full_name":"Crublet, Elodie","last_name":"Crublet"},{"full_name":"Debled, Elisa Colas","last_name":"Debled","first_name":"Elisa Colas"},{"last_name":"Moriscot","full_name":"Moriscot, Christine","first_name":"Christine"},{"last_name":"Gans","full_name":"Gans, Pierre","first_name":"Pierre"},{"first_name":"Guy","last_name":"Schoehn","full_name":"Schoehn, Guy"},{"full_name":"Macek, Pavel","last_name":"Macek","first_name":"Pavel"},{"last_name":"Schanda","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"},{"first_name":"Jerome","full_name":"Boisbouvier, Jerome","last_name":"Boisbouvier"}],"user_id":"3E5EF7F0-F248-11E8-B48F-1D18A9856A87","article_number":"eaau4196","publication":"Science Advances","language":[{"iso":"eng"}],"day":"19","month":"09","year":"2018","doi":"10.1126/sciadv.aau4196","date_published":"2018-09-19T00:00:00Z","date_updated":"2022-08-26T09:11:06Z","intvolume":"         4","publisher":"American Association for the Advancement of Science","citation":{"chicago":"Mas, Guillaume, Jia-Ying Guan, Elodie Crublet, Elisa Colas Debled, Christine Moriscot, Pierre Gans, Guy Schoehn, Pavel Macek, Paul Schanda, and Jerome Boisbouvier. “Structural Investigation of a Chaperonin in Action Reveals How Nucleotide Binding Regulates the Functional Cycle.” <i>Science Advances</i>. American Association for the Advancement of Science, 2018. <a href=\"https://doi.org/10.1126/sciadv.aau4196\">https://doi.org/10.1126/sciadv.aau4196</a>.","mla":"Mas, Guillaume, et al. “Structural Investigation of a Chaperonin in Action Reveals How Nucleotide Binding Regulates the Functional Cycle.” <i>Science Advances</i>, vol. 4, no. 9, eaau4196, American Association for the Advancement of Science, 2018, doi:<a href=\"https://doi.org/10.1126/sciadv.aau4196\">10.1126/sciadv.aau4196</a>.","short":"G. Mas, J.-Y. Guan, E. Crublet, E.C. Debled, C. Moriscot, P. Gans, G. Schoehn, P. Macek, P. Schanda, J. Boisbouvier, Science Advances 4 (2018).","apa":"Mas, G., Guan, J.-Y., Crublet, E., Debled, E. C., Moriscot, C., Gans, P., … Boisbouvier, J. (2018). Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle. <i>Science Advances</i>. American Association for the Advancement of Science. <a href=\"https://doi.org/10.1126/sciadv.aau4196\">https://doi.org/10.1126/sciadv.aau4196</a>","ama":"Mas G, Guan J-Y, Crublet E, et al. Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle. <i>Science Advances</i>. 2018;4(9). doi:<a href=\"https://doi.org/10.1126/sciadv.aau4196\">10.1126/sciadv.aau4196</a>","ista":"Mas G, Guan J-Y, Crublet E, Debled EC, Moriscot C, Gans P, Schoehn G, Macek P, Schanda P, Boisbouvier J. 2018. Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle. Science Advances. 4(9), eaau4196.","ieee":"G. Mas <i>et al.</i>, “Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle,” <i>Science Advances</i>, vol. 4, no. 9. American Association for the Advancement of Science, 2018."},"_id":"8437","abstract":[{"lang":"eng","text":"Chaperonins are ubiquitous protein assemblies present in bacteria, eukaryota, and archaea, facilitating the folding of proteins, preventing protein aggregation, and thus participating in maintaining protein homeostasis in the cell. During their functional cycle, they bind unfolded client proteins inside their double ring structure and promote protein folding by closing the ring chamber in an adenosine 5′-triphosphate (ATP)–dependent manner. Although the static structures of fully open and closed forms of chaperonins were solved by x-ray crystallography or electron microscopy, elucidating the mechanisms of such ATP-driven molecular events requires studying the proteins at the structural level under working conditions. We introduce an approach that combines site-specific nuclear magnetic resonance observation of very large proteins, enabled by advanced isotope labeling methods, with an in situ ATP regeneration system. Using this method, we provide functional insight into the 1-MDa large hsp60 chaperonin while processing client proteins and reveal how nucleotide binding, hydrolysis, and release control switching between closed and open states. While the open conformation stabilizes the unfolded state of client proteins, the internalization of the client protein inside the chaperonin cavity speeds up its functional cycle. This approach opens new perspectives to study structures and mechanisms of various ATP-driven biological machineries in the heat of action."}],"volume":4,"quality_controlled":"1","date_created":"2020-09-18T10:04:51Z","status":"public","publication_status":"published","oa_version":"None","type":"journal_article","extern":"1","article_type":"original","title":"Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle","issue":"9","article_processing_charge":"No"},{"day":"03","language":[{"iso":"eng"}],"month":"09","publication_identifier":{"issn":["1545-9993","1545-9985"]},"author":[{"first_name":"Vilius","full_name":"Kurauskas, Vilius","last_name":"Kurauskas"},{"first_name":"Audrey","full_name":"Hessel, Audrey","last_name":"Hessel"},{"last_name":"Dehez","full_name":"Dehez, François","first_name":"François"},{"full_name":"Chipot, Christophe","last_name":"Chipot","first_name":"Christophe"},{"first_name":"Beate","full_name":"Bersch, Beate","last_name":"Bersch"},{"first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","last_name":"Schanda"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","page":"745-747","publication":"Nature Structural & Molecular Biology","date_published":"2018-09-03T00:00:00Z","doi":"10.1038/s41594-018-0127-4","date_updated":"2021-01-12T08:19:16Z","intvolume":"        25","year":"2018","volume":25,"quality_controlled":"1","date_created":"2020-09-18T10:04:59Z","publisher":"Springer Nature","citation":{"short":"V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, P. Schanda, Nature Structural &#38; Molecular Biology 25 (2018) 745–747.","mla":"Kurauskas, Vilius, et al. “Dynamics and Interactions of AAC3 in DPC Are Not Functionally Relevant.” <i>Nature Structural &#38; Molecular Biology</i>, vol. 25, no. 9, Springer Nature, 2018, pp. 745–47, doi:<a href=\"https://doi.org/10.1038/s41594-018-0127-4\">10.1038/s41594-018-0127-4</a>.","chicago":"Kurauskas, Vilius, Audrey Hessel, François Dehez, Christophe Chipot, Beate Bersch, and Paul Schanda. “Dynamics and Interactions of AAC3 in DPC Are Not Functionally Relevant.” <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1038/s41594-018-0127-4\">https://doi.org/10.1038/s41594-018-0127-4</a>.","ista":"Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. 2018. Dynamics and interactions of AAC3 in DPC are not functionally relevant. Nature Structural &#38; Molecular Biology. 25(9), 745–747.","ieee":"V. Kurauskas, A. Hessel, F. Dehez, C. Chipot, B. Bersch, and P. Schanda, “Dynamics and interactions of AAC3 in DPC are not functionally relevant,” <i>Nature Structural &#38; Molecular Biology</i>, vol. 25, no. 9. Springer Nature, pp. 745–747, 2018.","apa":"Kurauskas, V., Hessel, A., Dehez, F., Chipot, C., Bersch, B., &#38; Schanda, P. (2018). Dynamics and interactions of AAC3 in DPC are not functionally relevant. <i>Nature Structural &#38; Molecular Biology</i>. Springer Nature. <a href=\"https://doi.org/10.1038/s41594-018-0127-4\">https://doi.org/10.1038/s41594-018-0127-4</a>","ama":"Kurauskas V, Hessel A, Dehez F, Chipot C, Bersch B, Schanda P. Dynamics and interactions of AAC3 in DPC are not functionally relevant. <i>Nature Structural &#38; Molecular Biology</i>. 2018;25(9):745-747. doi:<a href=\"https://doi.org/10.1038/s41594-018-0127-4\">10.1038/s41594-018-0127-4</a>"},"_id":"8438","keyword":["Molecular Biology","Structural Biology"],"extern":"1","article_type":"letter_note","title":"Dynamics and interactions of AAC3 in DPC are not functionally relevant","issue":"9","article_processing_charge":"No","status":"public","publication_status":"published","type":"journal_article","oa_version":"None"},{"doi":"10.1021/acschembio.8b00271","date_published":"2018-07-02T00:00:00Z","intvolume":"        13","date_updated":"2021-01-12T08:19:16Z","year":"2018","day":"02","language":[{"iso":"eng"}],"month":"07","author":[{"first_name":"Cedric","full_name":"Laguri, Cedric","last_name":"Laguri"},{"first_name":"Alba","full_name":"Silipo, Alba","last_name":"Silipo"},{"first_name":"Alessandra M.","last_name":"Martorana","full_name":"Martorana, Alessandra M."},{"last_name":"Schanda","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul"},{"first_name":"Roberta","last_name":"Marchetti","full_name":"Marchetti, Roberta"},{"full_name":"Polissi, Alessandra","last_name":"Polissi","first_name":"Alessandra"},{"last_name":"Molinaro","full_name":"Molinaro, Antonio","first_name":"Antonio"},{"full_name":"Simorre, Jean-Pierre","last_name":"Simorre","first_name":"Jean-Pierre"}],"publication_identifier":{"issn":["1554-8929","1554-8937"]},"page":"2106-2113","publication":"ACS Chemical Biology","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","article_type":"original","extern":"1","issue":"8","article_processing_charge":"No","title":"Solid state NMR studies of intact lipopolysaccharide endotoxin","publication_status":"published","status":"public","oa_version":"None","type":"journal_article","abstract":[{"text":"Lipopolysaccharides (LPS) are complex glycolipids forming the outside layer of Gram-negative bacteria. Their hydrophobic and heterogeneous nature greatly hampers their structural study in an environment similar to the bacterial surface. We have studied LPS purified from E. coli and pathogenic P. aeruginosa with long O-antigen polysaccharides assembled in solution as vesicles or elongated micelles. Solid-state NMR with magic-angle spinning permitted the identification of NMR signals arising from regions with different flexibilities in the LPS, from the lipid components to the O-antigen polysaccharides. Atomic scale data on the LPS enabled the study of the interaction of gentamicin antibiotic bound to P. aeruginosa LPS, for which we could confirm that a specific oligosaccharide is involved in the antibiotic binding. The possibility to study LPS alone and bound to a ligand when it is assembled in membrane-like structures opens great prospects for the investigation of proteins and antibiotics that specifically target such an important molecule at the surface of Gram-negative bacteria.","lang":"eng"}],"date_created":"2020-09-18T10:05:09Z","quality_controlled":"1","volume":13,"citation":{"ista":"Laguri C, Silipo A, Martorana AM, Schanda P, Marchetti R, Polissi A, Molinaro A, Simorre J-P. 2018. Solid state NMR studies of intact lipopolysaccharide endotoxin. ACS Chemical Biology. 13(8), 2106–2113.","ieee":"C. Laguri <i>et al.</i>, “Solid state NMR studies of intact lipopolysaccharide endotoxin,” <i>ACS Chemical Biology</i>, vol. 13, no. 8. American Chemical Society, pp. 2106–2113, 2018.","apa":"Laguri, C., Silipo, A., Martorana, A. M., Schanda, P., Marchetti, R., Polissi, A., … Simorre, J.-P. (2018). Solid state NMR studies of intact lipopolysaccharide endotoxin. <i>ACS Chemical Biology</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acschembio.8b00271\">https://doi.org/10.1021/acschembio.8b00271</a>","ama":"Laguri C, Silipo A, Martorana AM, et al. Solid state NMR studies of intact lipopolysaccharide endotoxin. <i>ACS Chemical Biology</i>. 2018;13(8):2106-2113. doi:<a href=\"https://doi.org/10.1021/acschembio.8b00271\">10.1021/acschembio.8b00271</a>","short":"C. Laguri, A. Silipo, A.M. Martorana, P. Schanda, R. Marchetti, A. Polissi, A. Molinaro, J.-P. Simorre, ACS Chemical Biology 13 (2018) 2106–2113.","chicago":"Laguri, Cedric, Alba Silipo, Alessandra M. Martorana, Paul Schanda, Roberta Marchetti, Alessandra Polissi, Antonio Molinaro, and Jean-Pierre Simorre. “Solid State NMR Studies of Intact Lipopolysaccharide Endotoxin.” <i>ACS Chemical Biology</i>. American Chemical Society, 2018. <a href=\"https://doi.org/10.1021/acschembio.8b00271\">https://doi.org/10.1021/acschembio.8b00271</a>.","mla":"Laguri, Cedric, et al. “Solid State NMR Studies of Intact Lipopolysaccharide Endotoxin.” <i>ACS Chemical Biology</i>, vol. 13, no. 8, American Chemical Society, 2018, pp. 2106–13, doi:<a href=\"https://doi.org/10.1021/acschembio.8b00271\">10.1021/acschembio.8b00271</a>."},"_id":"8439","publisher":"American Chemical Society","keyword":["Molecular Medicine","Biochemistry","General Medicine"]},{"year":"2018","intvolume":"       293","date_updated":"2021-01-12T08:19:17Z","date_published":"2018-06-01T00:00:00Z","doi":"10.1074/jbc.ra118.002251","publication":"Journal of Biological Chemistry","page":"8379-8393","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","author":[{"last_name":"Weinhäupl","full_name":"Weinhäupl, Katharina","first_name":"Katharina"},{"first_name":"Martha","full_name":"Brennich, Martha","last_name":"Brennich"},{"full_name":"Kazmaier, Uli","last_name":"Kazmaier","first_name":"Uli"},{"first_name":"Joel","full_name":"Lelievre, Joel","last_name":"Lelievre"},{"full_name":"Ballell, Lluis","last_name":"Ballell","first_name":"Lluis"},{"first_name":"Alfred","last_name":"Goldberg","full_name":"Goldberg, Alfred"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","last_name":"Schanda"},{"last_name":"Fraga","full_name":"Fraga, Hugo","first_name":"Hugo"}],"publication_identifier":{"issn":["0021-9258","1083-351X"]},"month":"06","language":[{"iso":"eng"}],"day":"01","oa_version":"None","type":"journal_article","status":"public","publication_status":"published","issue":"22","article_processing_charge":"No","title":"The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis","article_type":"original","extern":"1","keyword":["Cell Biology","Biochemistry","Molecular Biology"],"_id":"8440","citation":{"apa":"Weinhäupl, K., Brennich, M., Kazmaier, U., Lelievre, J., Ballell, L., Goldberg, A., … Fraga, H. (2018). The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology. <a href=\"https://doi.org/10.1074/jbc.ra118.002251\">https://doi.org/10.1074/jbc.ra118.002251</a>","ama":"Weinhäupl K, Brennich M, Kazmaier U, et al. The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. <i>Journal of Biological Chemistry</i>. 2018;293(22):8379-8393. doi:<a href=\"https://doi.org/10.1074/jbc.ra118.002251\">10.1074/jbc.ra118.002251</a>","ista":"Weinhäupl K, Brennich M, Kazmaier U, Lelievre J, Ballell L, Goldberg A, Schanda P, Fraga H. 2018. The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis. Journal of Biological Chemistry. 293(22), 8379–8393.","ieee":"K. Weinhäupl <i>et al.</i>, “The antibiotic cyclomarin blocks arginine-phosphate–induced millisecond dynamics in the N-terminal domain of ClpC1 from Mycobacterium tuberculosis,” <i>Journal of Biological Chemistry</i>, vol. 293, no. 22. American Society for Biochemistry &#38; Molecular Biology, pp. 8379–8393, 2018.","mla":"Weinhäupl, Katharina, et al. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.” <i>Journal of Biological Chemistry</i>, vol. 293, no. 22, American Society for Biochemistry &#38; Molecular Biology, 2018, pp. 8379–93, doi:<a href=\"https://doi.org/10.1074/jbc.ra118.002251\">10.1074/jbc.ra118.002251</a>.","chicago":"Weinhäupl, Katharina, Martha Brennich, Uli Kazmaier, Joel Lelievre, Lluis Ballell, Alfred Goldberg, Paul Schanda, and Hugo Fraga. “The Antibiotic Cyclomarin Blocks Arginine-Phosphate–Induced Millisecond Dynamics in the N-Terminal Domain of ClpC1 from Mycobacterium Tuberculosis.” <i>Journal of Biological Chemistry</i>. American Society for Biochemistry &#38; Molecular Biology, 2018. <a href=\"https://doi.org/10.1074/jbc.ra118.002251\">https://doi.org/10.1074/jbc.ra118.002251</a>.","short":"K. Weinhäupl, M. Brennich, U. Kazmaier, J. Lelievre, L. Ballell, A. Goldberg, P. Schanda, H. Fraga, Journal of Biological Chemistry 293 (2018) 8379–8393."},"publisher":"American Society for Biochemistry & Molecular Biology","date_created":"2020-09-18T10:05:18Z","volume":293,"quality_controlled":"1","abstract":[{"lang":"eng","text":"Mycobacterium tuberculosis can remain dormant in the host, an ability that explains the failure of many current tuberculosis treatments. Recently, the natural products cyclomarin, ecumicin, and lassomycin have been shown to efficiently kill Mycobacterium tuberculosis persisters. Their target is the N-terminal domain of the hexameric AAA+ ATPase ClpC1, which recognizes, unfolds, and translocates protein substrates, such as proteins containing phosphorylated arginine residues, to the ClpP1P2 protease for degradation. Surprisingly, these antibiotics do not inhibit ClpC1 ATPase activity, and how they cause cell death is still unclear. Here, using NMR and small-angle X-ray scattering, we demonstrate that arginine-phosphate binding to the ClpC1 N-terminal domain induces millisecond dynamics. We show that these dynamics are caused by conformational changes and do not result from unfolding or oligomerization of this domain. Cyclomarin binding to this domain specifically blocked these N-terminal dynamics. On the basis of these results, we propose a mechanism of action involving cyclomarin-induced restriction of ClpC1 dynamics, which modulates the chaperone enzymatic activity leading eventually to cell death."}]},{"publisher":"Springer Nature","citation":{"ieee":"A. Krushelnitsky, D. Gauto, D. C. Rodriguez Camargo, P. Schanda, and K. Saalwächter, “Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals,” <i>Journal of Biomolecular NMR</i>, vol. 71, no. 1. Springer Nature, pp. 53–67, 2018.","ista":"Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K. 2018. Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals. Journal of Biomolecular NMR. 71(1), 53–67.","ama":"Krushelnitsky A, Gauto D, Rodriguez Camargo DC, Schanda P, Saalwächter K. Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals. <i>Journal of Biomolecular NMR</i>. 2018;71(1):53-67. doi:<a href=\"https://doi.org/10.1007/s10858-018-0191-4\">10.1007/s10858-018-0191-4</a>","apa":"Krushelnitsky, A., Gauto, D., Rodriguez Camargo, D. C., Schanda, P., &#38; Saalwächter, K. (2018). Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals. <i>Journal of Biomolecular NMR</i>. Springer Nature. <a href=\"https://doi.org/10.1007/s10858-018-0191-4\">https://doi.org/10.1007/s10858-018-0191-4</a>","short":"A. Krushelnitsky, D. Gauto, D.C. Rodriguez Camargo, P. Schanda, K. Saalwächter, Journal of Biomolecular NMR 71 (2018) 53–67.","chicago":"Krushelnitsky, Alexey, Diego Gauto, Diana C. Rodriguez Camargo, Paul Schanda, and Kay Saalwächter. “Microsecond Motions Probed by Near-Rotary-Resonance R1ρ 15N MAS NMR Experiments: The Model Case of Protein Overall-Rocking in Crystals.” <i>Journal of Biomolecular NMR</i>. Springer Nature, 2018. <a href=\"https://doi.org/10.1007/s10858-018-0191-4\">https://doi.org/10.1007/s10858-018-0191-4</a>.","mla":"Krushelnitsky, Alexey, et al. “Microsecond Motions Probed by Near-Rotary-Resonance R1ρ 15N MAS NMR Experiments: The Model Case of Protein Overall-Rocking in Crystals.” <i>Journal of Biomolecular NMR</i>, vol. 71, no. 1, Springer Nature, 2018, pp. 53–67, doi:<a href=\"https://doi.org/10.1007/s10858-018-0191-4\">10.1007/s10858-018-0191-4</a>."},"_id":"8441","quality_controlled":"1","volume":71,"date_created":"2020-09-18T10:05:28Z","abstract":[{"lang":"eng","text":"Solid-state near-rotary-resonance measurements of the spin–lattice relaxation rate in the rotating frame (R1ρ) is a powerful NMR technique for studying molecular dynamics in the microsecond time scale. The small difference between the spin-lock (SL) and magic-angle-spinning (MAS) frequencies allows sampling very slow motions, at the same time it brings up some methodological challenges. In this work, several issues affecting correct measurements and analysis of 15N R1ρ data are considered in detail. Among them are signal amplitude as a function of the difference between SL and MAS frequencies, “dead time” in the initial part of the relaxation decay caused by transient spin-dynamic oscillations, measurements under HORROR condition and proper treatment of the multi-exponential relaxation decays. The multiple 15N R1ρ measurements at different SL fields and temperatures have been conducted in 1D mode (i.e. without site-specific resolution) for a set of four different microcrystalline protein samples (GB1, SH3, MPD-ubiquitin and cubic-PEG-ubiquitin) to study the overall protein rocking in a crystal. While the amplitude of this motion varies very significantly, its correlation time for all four sample is practically the same, 30–50 μs. The amplitude of the rocking motion correlates with the packing density of a protein crystal. It has been suggested that the rocking motion is not diffusive but likely a jump-like dynamic process."}],"oa_version":"Published Version","type":"journal_article","publication_status":"published","status":"public","title":"Microsecond motions probed by near-rotary-resonance R1ρ 15N MAS NMR experiments: The model case of protein overall-rocking in crystals","article_processing_charge":"No","issue":"1","extern":"1","article_type":"original","user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","page":"53-67","publication":"Journal of Biomolecular NMR","publication_identifier":{"issn":["0925-2738","1573-5001"]},"author":[{"last_name":"Krushelnitsky","full_name":"Krushelnitsky, Alexey","first_name":"Alexey"},{"full_name":"Gauto, Diego","last_name":"Gauto","first_name":"Diego"},{"first_name":"Diana C.","full_name":"Rodriguez Camargo, Diana C.","last_name":"Rodriguez Camargo"},{"id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul","last_name":"Schanda","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606"},{"full_name":"Saalwächter, Kay","last_name":"Saalwächter","first_name":"Kay"}],"month":"05","language":[{"iso":"eng"}],"day":"30","year":"2018","date_updated":"2021-01-12T08:19:17Z","intvolume":"        71","date_published":"2018-05-30T00:00:00Z","doi":"10.1007/s10858-018-0191-4"},{"language":[{"iso":"eng"}],"day":"28","month":"02","publication_identifier":{"issn":["0009-2665","1520-6890"]},"author":[{"last_name":"Chipot","full_name":"Chipot, Christophe","first_name":"Christophe"},{"full_name":"Dehez, François","last_name":"Dehez","first_name":"François"},{"first_name":"Jason R.","full_name":"Schnell, Jason R.","last_name":"Schnell"},{"first_name":"Nicole","last_name":"Zitzmann","full_name":"Zitzmann, Nicole"},{"first_name":"Eva","last_name":"Pebay-Peyroula","full_name":"Pebay-Peyroula, Eva"},{"first_name":"Laurent J.","full_name":"Catoire, Laurent J.","last_name":"Catoire"},{"first_name":"Bruno","full_name":"Miroux, Bruno","last_name":"Miroux"},{"full_name":"Kunji, Edmund R. S.","last_name":"Kunji","first_name":"Edmund R. S."},{"last_name":"Veglia","full_name":"Veglia, Gianluigi","first_name":"Gianluigi"},{"first_name":"Timothy A.","last_name":"Cross","full_name":"Cross, Timothy A."},{"orcid":"0000-0002-9350-7606","full_name":"Schanda, Paul","last_name":"Schanda","id":"7B541462-FAF6-11E9-A490-E8DFE5697425","first_name":"Paul"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","page":"3559-3607","publication":"Chemical Reviews","date_published":"2018-02-28T00:00:00Z","doi":"10.1021/acs.chemrev.7b00570","date_updated":"2021-01-12T08:19:18Z","intvolume":"       118","year":"2018","abstract":[{"text":"Membrane proteins perform a host of vital cellular functions. Deciphering the molecular mechanisms whereby they fulfill these functions requires detailed biophysical and structural investigations. Detergents have proven pivotal to extract the protein from its native surroundings. Yet, they provide a milieu that departs significantly from that of the biological membrane, to the extent that the structure, the dynamics, and the interactions of membrane proteins in detergents may considerably vary, as compared to the native environment. Understanding the impact of detergents on membrane proteins is, therefore, crucial to assess the biological relevance of results obtained in detergents. Here, we review the strengths and weaknesses of alkyl phosphocholines (or foscholines), the most widely used detergent in solution-NMR studies of membrane proteins. While this class of detergents is often successful for membrane protein solubilization, a growing list of examples points to destabilizing and denaturing properties, in particular for α-helical membrane proteins. Our comprehensive analysis stresses the importance of stringent controls when working with this class of detergents and when analyzing the structure and dynamics of membrane proteins in alkyl phosphocholine detergents.","lang":"eng"}],"quality_controlled":"1","volume":118,"date_created":"2020-09-18T10:05:35Z","publisher":"American Chemical Society","_id":"8442","citation":{"ama":"Chipot C, Dehez F, Schnell JR, et al. Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. <i>Chemical Reviews</i>. 2018;118(7):3559-3607. doi:<a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">10.1021/acs.chemrev.7b00570</a>","apa":"Chipot, C., Dehez, F., Schnell, J. R., Zitzmann, N., Pebay-Peyroula, E., Catoire, L. J., … Schanda, P. (2018). Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. <i>Chemical Reviews</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">https://doi.org/10.1021/acs.chemrev.7b00570</a>","ieee":"C. Chipot <i>et al.</i>, “Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies,” <i>Chemical Reviews</i>, vol. 118, no. 7. American Chemical Society, pp. 3559–3607, 2018.","ista":"Chipot C, Dehez F, Schnell JR, Zitzmann N, Pebay-Peyroula E, Catoire LJ, Miroux B, Kunji ERS, Veglia G, Cross TA, Schanda P. 2018. Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies. Chemical Reviews. 118(7), 3559–3607.","mla":"Chipot, Christophe, et al. “Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.” <i>Chemical Reviews</i>, vol. 118, no. 7, American Chemical Society, 2018, pp. 3559–607, doi:<a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">10.1021/acs.chemrev.7b00570</a>.","chicago":"Chipot, Christophe, François Dehez, Jason R. Schnell, Nicole Zitzmann, Eva Pebay-Peyroula, Laurent J. Catoire, Bruno Miroux, et al. “Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.” <i>Chemical Reviews</i>. American Chemical Society, 2018. <a href=\"https://doi.org/10.1021/acs.chemrev.7b00570\">https://doi.org/10.1021/acs.chemrev.7b00570</a>.","short":"C. Chipot, F. Dehez, J.R. Schnell, N. Zitzmann, E. Pebay-Peyroula, L.J. Catoire, B. Miroux, E.R.S. Kunji, G. Veglia, T.A. Cross, P. Schanda, Chemical Reviews 118 (2018) 3559–3607."},"keyword":["General Chemistry"],"extern":"1","article_type":"original","title":"Perturbations of native membrane protein structure in alkyl phosphocholine detergents: A critical assessment of NMR and biophysical studies","issue":"7","article_processing_charge":"No","publication_status":"published","status":"public","oa_version":"None","type":"journal_article"},{"date_updated":"2021-01-12T08:19:18Z","intvolume":"         9","date_published":"2018-02-03T00:00:00Z","doi":"10.1021/acs.jpclett.8b00269","year":"2018","month":"02","day":"03","language":[{"iso":"eng"}],"user_id":"2DF688A6-F248-11E8-B48F-1D18A9856A87","page":"933-938","publication":"The Journal of Physical Chemistry Letters","publication_identifier":{"issn":["1948-7185"]},"author":[{"full_name":"Kurauskas, Vilius","last_name":"Kurauskas","first_name":"Vilius"},{"first_name":"Audrey","full_name":"Hessel, Audrey","last_name":"Hessel"},{"first_name":"Peixiang","last_name":"Ma","full_name":"Ma, Peixiang"},{"last_name":"Lunetti","full_name":"Lunetti, Paola","first_name":"Paola"},{"last_name":"Weinhäupl","full_name":"Weinhäupl, Katharina","first_name":"Katharina"},{"first_name":"Lionel","full_name":"Imbert, Lionel","last_name":"Imbert"},{"last_name":"Brutscher","full_name":"Brutscher, Bernhard","first_name":"Bernhard"},{"full_name":"King, Martin S.","last_name":"King","first_name":"Martin S."},{"first_name":"Rémy","full_name":"Sounier, Rémy","last_name":"Sounier"},{"last_name":"Dolce","full_name":"Dolce, Vincenza","first_name":"Vincenza"},{"first_name":"Edmund R. S.","last_name":"Kunji","full_name":"Kunji, Edmund R. S."},{"first_name":"Loredana","last_name":"Capobianco","full_name":"Capobianco, Loredana"},{"last_name":"Chipot","full_name":"Chipot, Christophe","first_name":"Christophe"},{"last_name":"Dehez","full_name":"Dehez, François","first_name":"François"},{"full_name":"Bersch, Beate","last_name":"Bersch","first_name":"Beate"},{"last_name":"Schanda","full_name":"Schanda, Paul","orcid":"0000-0002-9350-7606","first_name":"Paul","id":"7B541462-FAF6-11E9-A490-E8DFE5697425"}],"title":"How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine","article_processing_charge":"No","issue":"5","extern":"1","article_type":"original","type":"journal_article","oa_version":"None","publication_status":"published","status":"public","volume":9,"quality_controlled":"1","date_created":"2020-09-18T10:05:45Z","abstract":[{"text":"Characterizing the structure of membrane proteins (MPs) generally requires extraction from their native environment, most commonly with detergents. Yet, the physicochemical properties of detergent micelles and lipid bilayers differ markedly and could alter the structural organization of MPs, albeit without general rules. Dodecylphosphocholine (DPC) is the most widely used detergent for MP structure determination by NMR, but the physiological relevance of several prominent structures has been questioned, though indirectly, by other biophysical techniques, e.g., functional/thermostability assay (TSA) and molecular dynamics (MD) simulations. Here, we resolve unambiguously this controversy by probing the functional relevance of three different mitochondrial carriers (MCs) in DPC at the atomic level, using an exhaustive set of solution-NMR experiments, complemented by functional/TSA and MD data. Our results provide atomic-level insight into the structure, substrate interaction and dynamics of the detergent–membrane protein complexes and demonstrates cogently that, while high-resolution NMR signals can be obtained for MCs in DPC, they systematically correspond to nonfunctional states.","lang":"eng"}],"keyword":["General Materials Science"],"publisher":"American Chemical Society","_id":"8443","citation":{"short":"V. Kurauskas, A. Hessel, P. Ma, P. Lunetti, K. Weinhäupl, L. Imbert, B. Brutscher, M.S. King, R. Sounier, V. Dolce, E.R.S. Kunji, L. Capobianco, C. Chipot, F. Dehez, B. Bersch, P. Schanda, The Journal of Physical Chemistry Letters 9 (2018) 933–938.","chicago":"Kurauskas, Vilius, Audrey Hessel, Peixiang Ma, Paola Lunetti, Katharina Weinhäupl, Lionel Imbert, Bernhard Brutscher, et al. “How Detergent Impacts Membrane Proteins: Atomic-Level Views of Mitochondrial Carriers in Dodecylphosphocholine.” <i>The Journal of Physical Chemistry Letters</i>. American Chemical Society, 2018. <a href=\"https://doi.org/10.1021/acs.jpclett.8b00269\">https://doi.org/10.1021/acs.jpclett.8b00269</a>.","mla":"Kurauskas, Vilius, et al. “How Detergent Impacts Membrane Proteins: Atomic-Level Views of Mitochondrial Carriers in Dodecylphosphocholine.” <i>The Journal of Physical Chemistry Letters</i>, vol. 9, no. 5, American Chemical Society, 2018, pp. 933–38, doi:<a href=\"https://doi.org/10.1021/acs.jpclett.8b00269\">10.1021/acs.jpclett.8b00269</a>.","ieee":"V. Kurauskas <i>et al.</i>, “How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine,” <i>The Journal of Physical Chemistry Letters</i>, vol. 9, no. 5. American Chemical Society, pp. 933–938, 2018.","ista":"Kurauskas V, Hessel A, Ma P, Lunetti P, Weinhäupl K, Imbert L, Brutscher B, King MS, Sounier R, Dolce V, Kunji ERS, Capobianco L, Chipot C, Dehez F, Bersch B, Schanda P. 2018. How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine. The Journal of Physical Chemistry Letters. 9(5), 933–938.","ama":"Kurauskas V, Hessel A, Ma P, et al. How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine. <i>The Journal of Physical Chemistry Letters</i>. 2018;9(5):933-938. doi:<a href=\"https://doi.org/10.1021/acs.jpclett.8b00269\">10.1021/acs.jpclett.8b00269</a>","apa":"Kurauskas, V., Hessel, A., Ma, P., Lunetti, P., Weinhäupl, K., Imbert, L., … Schanda, P. (2018). How detergent impacts membrane proteins: Atomic-level views of mitochondrial carriers in dodecylphosphocholine. <i>The Journal of Physical Chemistry Letters</i>. American Chemical Society. <a href=\"https://doi.org/10.1021/acs.jpclett.8b00269\">https://doi.org/10.1021/acs.jpclett.8b00269</a>"}}]